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dc.contributor.authorWang, Zhenyu
dc.contributor.authorYang, Bo
dc.contributor.authorZhang, Zhenqing
dc.contributor.authorLy, Mellisa
dc.contributor.authorTakieddin, Majde
dc.contributor.authorMousa, Shaker
dc.contributor.authorLiu, Jian
dc.contributor.authorDordick, Jonathan S.
dc.contributor.authorLinhardt, Robert J.
dc.date2011
dc.date.accessioned2022-06-23T04:11:28Z
dc.date.available2022-06-23T04:11:28Z
dc.date.issued2011-07-01
dc.identifier.citationControl of the heparosan N-deacetylation leads to an improved bioengineered heparin, Z. Wang, B. Yang, Z. Zhang, M. Ly, M. Takieddin, S. Mousa, J. Liu, J. S. Dordick, R. J. Linhardt Applied Microbiology and Biotechnology, 91, 91-99, 2011.
dc.identifier.issn14320614
dc.identifier.issn1757598
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5286
dc.identifier.urihttps://doi.org/10.1007/s00253-011-3231-5
dc.descriptionApplied Microbiology and Biotechnology, 91, 91-99
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractThe production of the anticoagulant drug heparin from non-animal sources has a number of advantages over the current commercial production of heparin. These advantages include better source material availability, improved quality control, and reduced concerns about animal virus or prion impurities. A bioengineered heparin would have to be chemically and biologically equivalent to be substituted for animal-sourced heparin as a pharmaceutical. In an effort to produce bioengineered heparin that more closely resembles pharmaceutical heparin, we have investigated a key step in the process involving the N-deacetylation of heparosan. The extent of N-deacetylation directly affects the N-acetyl/N-sulfo ratio in bioengineered heparin and also impacts its molecular weight. Previous studies have demonstrated that the presence and quantity of N-acetylglucosamine in the nascent glycosaminoglycan chain, serving as the substrate for the subsequent enzymatic modifications (C5 epimerization and O-sulfonation), can impact the action of these enzymes and, thus, the content and distribution of iduronic acid and O-sulfo groups. In this study, we control the N-deacetylation of heparosan to produce a bioengineered heparin with an N-acetyl/N-sulfo ratio and molecular weight that is similar to animal-sourced pharmaceutical heparin. The structural composition and anticoagulant activity of the resultant bioengineered heparin was extensively characterized and compared to pharmaceutical heparin obtained from porcine intestinal mucosa.
dc.description.sponsorshipNational Institutes of Health
dc.languageen_US
dc.language.isoENG
dc.publisherSpringer
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofApplied Microbiology and Biotechnology
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleControl of the heparosan N-deacetylation leads to an improved bioengineered heparin
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1007/s00253-011-3231-5
dc.rights.holderIn Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.pages91-99
rpi.description.volume91


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